Drosophila nemo was first identified as a gene required for tissue polarity during ommatidial development. We have extended the analysis of nemo and found that it participates in multiple developmental processes. It is required during wing development for wing shape and vein patterning. We observe genetic interactions between nemo and mutations in the Notch, Wingless, Frizzled and Decapentaplegic pathways. Our data support the findings from other organisms that Nemo proteins act as negative regulators of Wingless signaling. nemo mutations cause polarity defects in the adult wing and overexpression of nemo leads to abdominal polarity defects. The expression of nemo during embryogenesis is dynamic and dsRNA inhibition and ectopic expression studies indicate that nemo is essential during embryogenesis.
Potassium channels vary in their function and regulation, yet they maintain a number of important features - they are involved in the control of potassium flow, cell volume, cell membrane resting potential, cell excitability and hormone release. The potassium (K(+)) inward rectifier (Kir) superfamily of channels are potassium selective channels, that are sensitive to the concentration of K(+) ions. They are termed inward rectifiers since they allow a much greater K(+) influx than efflux. There are at least seven subfamilies of Kir channels, grouped according to sequence and functional similarities (Curr. Opin. Neurobiol. 5 (1995) 268; Annu. Rev. Physiol. 59 (1997) 171). While numerous Kir channels have been discovered in a variety of organisms, Drosophila inward rectifier (Dir) is the first putative inward rectifier to be studied in Drosophila. In fact, there are only three genes (including Dir) encoding putative inward rectifiers in the Drosophila genome. Though there are other known potassium channels in Drosophila such as ether-a-go-go and shaker, most are voltage-gated channels. As an important first step in characterizing Kir channels in Drosophila, we initiated studies on Dir.
A new light-chain marker has been detected in normal mouse serum immunoglobulin light chains by gel isoelectric focusing. The marker (Ef2) involves the presence of two major and several minor bands in the normal light-chain IF profiles. Strains expressing the marker IF bands are designated Igk-Ef2a, whereas those lacking the bands are Igk-Ef2b. The majority of inbred strains are Igk-Ef2a. Strains found to be Igk-Ef2b are NZB/BlNJ, BDP/J, C58/J, I/LnJ, CE/J, and P/J. The strain distribution of the alleles differs from the distribution of alleles at the Ly-2 and Ly-3 loci, suggesting the new marker may represent a separate locus. Genetic studies have shown that Igk-Ef2 locus is closely linked to Igk-Ef1 and Hd loci on Chromosome 6, indicating that it is also closely linked to Ly-3. The relative importance of the bands controlled by the Igk-Ef2 locus suggests that the entire normal light-chain pool could be controlled by as few as 100 such loci.
In this study we report the first instance of recombination between kappa chain genetic markers in the mouse. The recombination frequency, 0.45% (95% limits, 0.12-1.61), is similar to that previously found for recombination between the kappa chain locus and the Lyt-2,3 locus (0.3%, 95% limits, 0.05-1.6), but is relatively low in comparison with that found at the heavy chain locus (0.41-5.4%). Lyt-2,3-typing of the recombinants permits a partial ordering of the kappa chain and Lyt-2,3 loci as (Lyt-2,3, Igk-Ef1) - Igk-Ef2. Light chains controlled by the two kappa markers include the Vk-(ser) subgroup (controlled by Igk-Ef1) and Vk-1 (controlled by Igk-Ef2). One of the recombinants has been recovered in a homozygous state ("NAK") and should be suitable for Vk gene mapping studies.
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